Research workbench
Crystal structure of phosphorylated P38AMAPK in complex with TAB1
Analyse Crystal structure of phosphorylated P38AMAPK in complex with TAB1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NZZ
- Type
- protein
- Length
- 2,871 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 1; Mitogen-activated protein…
- EC
- 2.7.11.24
- UniProt
- Q15750, P47811
- Ligands
- AGS, NI, MG
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 8 distinct chains · 37% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 | protein | 378 | 36% helix, 23% strand | Q15750 |
| B | TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 | protein | 378 | 37% helix, 24% strand | Q15750 |
| C | TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 | protein | 367 | 37% helix, 25% strand | Q15750 |
| D | TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 | protein | 379 | 35% helix, 24% strand | Q15750 |
| E | Mitogen-activated protein kinase 14 (EC 2.7.11.24) | protein | 345 | 39% helix, 15% strand | P47811 |
| F | Mitogen-activated protein kinase 14 (EC 2.7.11.24) | protein | 343 | 38% helix, 14% strand | P47811 |
| G | Mitogen-activated protein kinase 14 (EC 2.7.11.24) | protein | 344 | 37% helix, 14% strand | P47811 |
| H | Mitogen-activated protein kinase 14 (EC 2.7.11.24) | protein | 337 | 35% helix, 14% strand | P47811 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 4 copies · chains E, F, G, H
- NI · Nickel (II) ion · metal · 6 copies · chains A, B, C, D, E, F
- MG · Magnesium ion · metal · 6 copies · chains E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 996 | 0.79 | 0.81 | 92 | empty |
| 2 | 974 | 0.78 | 0.81 | 93 | empty |
| 3 | 757 | 0.76 | 0.81 | 88 | empty |
| 4 | 638 | 0.74 | 0.80 | 69 | empty |
| 5 | 193 | 0.74 | 0.90 | 42 | empty |
Interfaces
13 interfaces between chains.
- A–F · 1095 Ų buried · 14 hydrogen bonds · protein-protein
- D–E · 1049 Ų buried · 11 hydrogen bonds · protein-protein
- B–G · 953 Ų buried · 9 hydrogen bonds · protein-protein
- C–H · 835 Ų buried · 8 hydrogen bonds · protein-protein
- B–E · 787 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 8 modified (phosphorylation).
Compared structures
- 5NZZ · Crystal structure of phosphorylated p38aMAPK in complex with TAB1 · the same entry in another collection · chain H against H, TM-score 1.00
- Q15750 · AlphaFold monomer V2.0 prediction for TGF-beta-activated kinase 1 and MAP3K7-binding… · a predicted model of the same protein · chain C against A, TM-score 0.96
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q15750
- Every structure of UniProt P47811
- Elsewhere: RCSB PDB 5NZZ · PDBe 5NZZ · UniProt Q15750 · UniProt P47811
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